The coiled-coil protein-binding motif in Fusarium verticillioides Fsr1 is essential for maize stalk rot virulence

Fusarium verticillioides (Sacc.) Nirenberg (teleomorph Gibberella moniliformis Wineland) is one of the key pathogens of maize stalk rot disease. However, a clear understanding of stalk rot pathogenesis is still lacking. Previously, we identified the F. verticillioides FSR1 gene, which plays a key role in fungal virulence and sexual mating. The predicted Fsr1 protein contains multiple protein-binding domains, namely a caveolin-binding domain, a coiled-coil structure, and a calmodulin-binding motif at the N terminus and a WD40 repeat domain at the C terminus. Fsr1 shares significant similarity to a family of striatin proteins that play a critical role in cellular mechanisms that regulate a variety of developmental processes. Significantly, FSR1 function is conserved in Fusarium graminearum, where it also plays a direct role in pathogenesis. In this study, our goal was to determine the motif(s) in Fsr1 that are directly associated with fungal virulence. We complemented the FSR1 knockout (Δfsr1) strain with mutated versions of the FSR1 gene, and determined that the Fsr1 C-terminal WD40 repeat domain is dispensable for vegetative growth and maize stalk rot virulence. We also examined the potential link between FSR1-mediated virulence and cell wall-degrading enzyme (α-amylase, pectinase and cellulase) activities. Further characterization of the N-terminal region revealed that the coiled-coil structure is essential for virulence in F. verticillioides. The coiled-coil domain is involved in a variety of protein-protein interactions in eukaryotic systems, and thus we hypothesize that the interaction between Fsr1 and the putative Fsr1 -binding protein triggers downstream gene signalling that is associated with F. verticillioides virulence.